Header list of 1kvj.pdb file
Complete list - 23 20 Bytes
HEADER HYDROLASE 26-JAN-02 1KVJ
TITLE SOLUTION STRUCTURE OF THE CU(I) BOUND FORM OF THE FIRST HEAVY METAL
TITLE 2 BINDING MOTIF OF THE MENKES PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COPPER-TRANSPORTING ATPASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-79;
COMPND 5 SYNONYM: MENKES DISEASE-ASSOCIATED PROTEIN;
COMPND 6 EC: 3.6.3.4;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMAL
KEYWDS MENKES, CU-BOUND, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR T.M.DE SILVA,G.VEGLIA,S.J.OPELLA
REVDAT 3 23-FEB-22 1KVJ 1 REMARK LINK
REVDAT 2 24-FEB-09 1KVJ 1 VERSN
REVDAT 1 18-NOV-03 1KVJ 0
JRNL AUTH T.M.DESILVA,G.VEGLIA,S.J.OPELLA
JRNL TITL SOLUTION STRUCTURES OF THE REDUCED AND CU(I) BOUND FORMS OF
JRNL TITL 2 THE FIRST METAL BINDING SEQUENCE OF ATP7A ASSOCIATED WITH
JRNL TITL 3 MENKES DISEASE.
JRNL REF PROTEINS V. 61 1038 2005
JRNL REFN ISSN 0887-3585
JRNL PMID 16211579
JRNL DOI 10.1002/PROT.20639
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KVJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-FEB-02.
REMARK 100 THE DEPOSITION ID IS D_1000015384.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 295
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 20 MM NA ACETATE BUFFER, 10 MM
REMARK 210 DTT, 1 MM EDTA, 0.01% NA AZIDE,
REMARK 210 1 MM PROTEIN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : UXNMR, NMRCOMPASS
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG1 THR A 18 HZ3 LYS A 46 1.30
REMARK 500 OE1 GLN A 28 HZ1 LYS A 32 1.37
REMARK 500 OG1 THR A 11 HG1 THR A 49 1.38
REMARK 500 HZ1 LYS A 60 OE1 GLU A 64 1.39
REMARK 500 O LEU A 43 HZ2 LYS A 46 1.40
REMARK 500 OD1 ASP A 53 HZ2 LYS A 55 1.44
REMARK 500 HG SER A 13 O VAL A 74 1.46
REMARK 500 HG1 THR A 61 OE2 GLU A 64 1.49
REMARK 500 HG SER A 42 OE1 GLU A 44 1.50
REMARK 500 O PRO A 3 HG SER A 4 1.52
REMARK 500 O GLY A 6 HZ3 LYS A 55 1.52
REMARK 500 H LYS A 40 O THR A 49 1.57
REMARK 500 O ASN A 8 H TYR A 52 1.58
REMARK 500 H ILE A 12 O ALA A 48 1.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 SER A 4 40.67 -177.43
REMARK 500 1 THR A 18 49.17 -71.59
REMARK 500 1 ASN A 20 -51.55 -14.97
REMARK 500 1 ASN A 34 -76.75 -163.04
REMARK 500 1 HIS A 38 121.10 -170.83
REMARK 500 1 PRO A 59 8.32 -62.78
REMARK 500 1 ASN A 77 -66.20 -109.93
REMARK 500 2 VAL A 7 158.40 69.08
REMARK 500 2 THR A 18 -27.65 -147.22
REMARK 500 2 ASN A 34 -52.13 -178.86
REMARK 500 2 LYS A 46 59.47 37.15
REMARK 500 2 ASP A 72 92.98 -56.62
REMARK 500 3 CYS A 19 139.33 -170.07
REMARK 500 3 ASN A 20 -45.44 -23.09
REMARK 500 3 ASN A 34 -32.14 -173.46
REMARK 500 3 ILE A 75 -135.56 -156.39
REMARK 500 3 HIS A 76 53.52 -103.70
REMARK 500 4 MET A 5 -61.28 62.79
REMARK 500 4 THR A 18 -48.50 61.51
REMARK 500 4 ASN A 20 -40.97 -29.28
REMARK 500 4 ASN A 34 -53.62 -179.58
REMARK 500 4 HIS A 38 122.88 -170.40
REMARK 500 5 MET A 17 97.49 -28.13
REMARK 500 5 CYS A 19 173.81 178.76
REMARK 500 5 ASN A 20 -36.65 -38.34
REMARK 500 5 ASN A 34 -66.77 -162.22
REMARK 500 5 ASP A 72 107.87 -48.39
REMARK 500 5 VAL A 74 103.72 -168.91
REMARK 500 5 ILE A 75 -137.83 -157.65
REMARK 500 5 HIS A 76 71.14 -104.65
REMARK 500 6 MET A 5 28.32 46.51
REMARK 500 6 VAL A 7 174.99 64.81
REMARK 500 6 THR A 18 -42.84 58.93
REMARK 500 6 CYS A 19 163.49 179.02
REMARK 500 6 ASN A 20 -36.71 -35.13
REMARK 500 6 ASN A 34 -60.38 -175.39
REMARK 500 6 PRO A 54 57.61 -67.63
REMARK 500 6 LYS A 55 -66.25 -135.47
REMARK 500 6 VAL A 74 -134.70 -117.51
REMARK 500 7 SER A 4 -22.49 -141.17
REMARK 500 7 VAL A 7 165.78 67.97
REMARK 500 7 CYS A 19 139.64 -178.99
REMARK 500 7 ASN A 20 -46.12 -23.08
REMARK 500 7 ASN A 34 -68.07 -169.66
REMARK 500 7 SER A 42 -101.04 -108.84
REMARK 500 7 LEU A 43 -92.41 -179.13
REMARK 500 7 PRO A 54 70.31 -64.67
REMARK 500 7 LYS A 55 -45.48 -172.24
REMARK 500 8 SER A 4 29.02 -156.01
REMARK 500 8 MET A 5 107.05 -41.45
REMARK 500
REMARK 500 THIS ENTRY HAS 72 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 A 85 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 19 O
REMARK 620 2 CYS A 19 SG 79.0
REMARK 620 3 SER A 21 OG 114.7 89.3
REMARK 620 4 CYS A 22 N 62.4 132.2 82.9
REMARK 620 5 CYS A 22 SG 99.6 145.2 121.5 72.6
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 A 85
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KVI RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE REDUCED FORM OF THE FIRST HEAVY METAL
REMARK 900 BINDING MOTIF OF THE MENKES PROTEIN
DBREF 1KVJ A 1 79 UNP Q04656 ATP7A_HUMAN 1 79
SEQRES 1 A 79 MET ASP PRO SER MET GLY VAL ASN SER VAL THR ILE SER
SEQRES 2 A 79 VAL GLU GLY MET THR CYS ASN SER CYS VAL TRP THR ILE
SEQRES 3 A 79 GLU GLN GLN ILE GLY LYS VAL ASN GLY VAL HIS HIS ILE
SEQRES 4 A 79 LYS VAL SER LEU GLU GLU LYS ASN ALA THR ILE ILE TYR
SEQRES 5 A 79 ASP PRO LYS LEU GLN THR PRO LYS THR LEU GLN GLU ALA
SEQRES 6 A 79 ILE ASP ASP MET GLY PHE ASP ALA VAL ILE HIS ASN PRO
SEQRES 7 A 79 ASP
HET CU1 A 85 1
HETNAM CU1 COPPER (I) ION
FORMUL 2 CU1 CU 1+
HELIX 1 1 ASN A 20 LYS A 32 1 13
HELIX 2 2 THR A 58 GLY A 70 1 13
SHEET 1 A 4 HIS A 38 SER A 42 0
SHEET 2 A 4 ASN A 47 TYR A 52 -1 O THR A 49 N LYS A 40
SHEET 3 A 4 ASN A 8 GLU A 15 -1 N ASN A 8 O TYR A 52
SHEET 4 A 4 ASP A 72 ILE A 75 -1 O VAL A 74 N SER A 13
LINK O CYS A 19 CU CU1 A 85 1555 1555 2.13
LINK SG CYS A 19 CU CU1 A 85 1555 1555 2.15
LINK OG SER A 21 CU CU1 A 85 1555 1555 1.97
LINK N CYS A 22 CU CU1 A 85 1555 1555 2.71
LINK SG CYS A 22 CU CU1 A 85 1555 1555 2.16
SITE 1 AC1 3 CYS A 19 SER A 21 CYS A 22
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - 23 20 Bytes